ID A0A1X7FA43_9PROT Unreviewed; 1035 AA.
AC A0A1X7FA43;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Tetrathionate reductase subunit A {ECO:0000313|EMBL:SMF49013.1};
GN ORFNames=SAMN02982917_2424 {ECO:0000313|EMBL:SMF49013.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF49013.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF49013.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF49013.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FXAK01000005; SMF49013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7FA43; -.
DR STRING; 286727.SAMN02982917_2424; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000192936; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR CDD; cd02758; MopB_Tetrathionate-Ra; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR041929; Tetrathionate-R_A_N.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1035
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013163336"
FT DOMAIN 70..156
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1035 AA; 111044 MW; 0988707453E12F31 CRC64;
MSITRRHILT STAAGGALAA FAGGFSETGR KLVKGAWAGE RPDDSISGNA PKPEFRIDPA
TGAVEPTPGQ IVANVACLGC TTLCGVRVRV DVERNRVLRV AGNPYSPLST DPFLPYATPI
EESFRSLSRL DEKGLQGRST ACGRGNAALE MLTSPFRITT PMKRVGPRGS GRWEPIAFDK
LVEEIAEGGD LFGEGPVEGL RTLRDLKTPI DPASPELGPK VNQVALLASV NDGREPFVRR
FFNQALGTIN FAGHGAYCGG AYRSGSGAAF GDLKAMPHAK PDLQNAEFVL FIGTAPSNAG
NPFKRQAMLV AKGRTDGVLN YVVVDPVLTN ADNRAAGERS NWIPIRPGTD GALVMGMMRW
MFENDRIDSR YLSQPNAKAA TAAGEAGWCN ATHLVIRQQG HLRDGRMLRA SDMGWIELDE
KERYGEKDAF VVLDPAGKPV AHDALGGPAV LFHDGAVATP TGDISVKTSL TLLREEAMRL
DLRGYAEACG IPADIIAGLA REFTSHGKKA VANAHGGMMA GNGFYNAFGV VTLNTLIGNL
NWKGGSIFGG GRFPDEQDGP RYKLASFPGA VKPSGTAINR PVPYEKSSEF ARNKAAGKPY
PAKAPWYPAA PQLTTEYLTS GLADGYPYRL KALFLWNSNP VYGIPGVRAA AEAAMKDPKT
LPLIVSIDPF INESSAFADY IVPDTVLYET WGWASPWGGV PTKTSTARWP VVEPRTQTLP
DGLHVQMETF LIALAKRLGL PGFGADAIAD MDGKLYPLDR PEDWYLRGGA NIAWLGKQPV
ADADDRDIAL SGVERVMPAL RATLKPEEWR KVAYILARGG RYQNQAEGFE GDKAAHKFLK
PLQVYNEAVG TAKSSITGRR WTGTATWMEP VFADGSPVHK HHTPEEWPFK LVSSKSVLVS
AYTIAAGRLR HLHPDNPVGI NAEDARRLGI ETGDRIRIAT PGGMREATAI VRHGVMRGVL
AVEHGFGHRE YGARPHLIGG HSQPSVPEIG AGINLNDLGI ADPSRAGASV WVDPIAGTAV
RQGIPAKLER LAASA
//
